ID   PDE6C_MOUSE             Reviewed;         861 AA.
AC   Q91ZQ1; Q8R0D4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 137.
DE   RecName: Full=Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha';
DE            EC=3.1.4.35 {ECO:0000250|UniProtKB:P51160};
DE   AltName: Full=cGMP phosphodiesterase 6C;
DE   Flags: Precursor;
GN   Name=Pde6c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RA   Chang B., Hawes N.L., Hurd R.E., Davisson M.T., Nusinowitz S.,
RA   Heckenlively J.R.;
RT   "A sequence alteration in Pde6c gene causes cone photoreceptor function
RT   loss (cpfl1) in mice.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: As cone-specific cGMP phosphodiesterase, it plays an
CC       essential role in light detection and cone phototransduction by rapidly
CC       decreasing intracellular levels of cGMP.
CC       {ECO:0000250|UniProtKB:P51160}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC         ChEBI:CHEBI:58115; EC=3.1.4.35;
CC         Evidence={ECO:0000250|UniProtKB:P51160};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions. {ECO:0000250};
CC   -!- SUBUNIT: Composed of two alpha' subunits that are associated with 3
CC       smaller proteins of 11, 13, and 15 kDa. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91ZQ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91ZQ1-2; Sequence=VSP_017422;
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF411063; AAK96254.1; -; mRNA.
DR   EMBL; BC027050; AAH27050.1; -; mRNA.
DR   CCDS; CCDS37971.1; -. [Q91ZQ1-1]
DR   CCDS; CCDS50431.1; -. [Q91ZQ1-2]
DR   RefSeq; NP_001164430.1; NM_001170959.1. [Q91ZQ1-2]
DR   RefSeq; NP_291092.1; NM_033614.2. [Q91ZQ1-1]
DR   AlphaFoldDB; Q91ZQ1; -.
DR   SMR; Q91ZQ1; -.
DR   BioGRID; 225961; 5.
DR   STRING; 10090.ENSMUSP00000025956; -.
DR   iPTMnet; Q91ZQ1; -.
DR   PhosphoSitePlus; Q91ZQ1; -.
DR   MaxQB; Q91ZQ1; -.
DR   PaxDb; 10090-ENSMUSP00000025956; -.
DR   ProteomicsDB; 287989; -. [Q91ZQ1-1]
DR   ProteomicsDB; 287990; -. [Q91ZQ1-2]
DR   Antibodypedia; 30485; 136 antibodies from 22 providers.
DR   DNASU; 110855; -.
DR   Ensembl; ENSMUST00000025956.13; ENSMUSP00000025956.6; ENSMUSG00000024992.14. [Q91ZQ1-1]
DR   Ensembl; ENSMUST00000112329.3; ENSMUSP00000107948.2; ENSMUSG00000024992.14. [Q91ZQ1-2]
DR   GeneID; 110855; -.
DR   KEGG; mmu:110855; -.
DR   UCSC; uc008hjf.2; mouse. [Q91ZQ1-1]
DR   UCSC; uc012blg.1; mouse. [Q91ZQ1-2]
DR   AGR; MGI:105956; -.
DR   CTD; 5146; -.
DR   MGI; MGI:105956; Pde6c.
DR   VEuPathDB; HostDB:ENSMUSG00000024992; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   GeneTree; ENSGT00940000157825; -.
DR   HOGENOM; CLU_006980_2_0_1; -.
DR   InParanoid; Q91ZQ1; -.
DR   OMA; LICNMMN; -.
DR   OrthoDB; 5479253at2759; -.
DR   PhylomeDB; Q91ZQ1; -.
DR   TreeFam; TF316499; -.
DR   BioGRID-ORCS; 110855; 1 hit in 77 CRISPR screens.
DR   ChiTaRS; Pde6c; mouse.
DR   PRO; PR:Q91ZQ1; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q91ZQ1; Protein.
DR   Bgee; ENSMUSG00000024992; Expressed in retinal neural layer and 26 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR   GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007603; P:phototransduction, visible light; IMP:MGI.
DR   GO; GO:0046549; P:retinal cone cell development; IMP:MGI.
DR   GO; GO:0050953; P:sensory perception of light stimulus; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   PANTHER; PTHR11347:SF23; CONE CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS00126; PDEASE_I_1; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
DR   Genevisible; Q91ZQ1; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; cGMP; cGMP-binding; Hydrolase;
KW   Lipoprotein; Membrane; Metal-binding; Methylation; Nucleotide-binding;
KW   Prenylation; Reference proteome; Repeat; Sensory transduction; Vision.
FT   CHAIN           1..858
FT                   /note="Cone cGMP-specific 3',5'-cyclic phosphodiesterase
FT                   subunit alpha'"
FT                   /id="PRO_0000226068"
FT   PROPEP          859..861
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370789"
FT   DOMAIN          75..224
FT                   /note="GAF 1"
FT   DOMAIN          256..433
FT                   /note="GAF 2"
FT   DOMAIN          486..819
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   REGION          826..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..852
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        562
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /evidence="ECO:0000250"
FT   BINDING         169..172
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /evidence="ECO:0000250"
FT   BINDING         566
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         602
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         603
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         603
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         723
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         858
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           858
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         737..761
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017422"
SQ   SEQUENCE   861 AA;  98785 MW;  C582D78114652B5B CRC64;
     MGEISQEAVE RYLEKNPCFA KEYFDKKLRV EALGVIFKNS HAGVQTGLSL PEMTQVEESA
     VCLELLQCMQ DEAGSAEQMA HRALQRLAQL LQADCCSMFS CRARNGIPEV ASRLLNVTPT
     SKFEDNLVAP DREVVFPLDI GIVGWVAHVK KALNVSDVKK NSHFSDFMDK QTGYVTRNLL
     AVPIVAGKEV LAVVMAVNKI SAPEFSKQDE EVFSKYLSFV AVALRLQHTS YLYSVESRRS
     QILMWSANKV FEELTDVERQ FHKALYTIRT YLNCDRYSIG LLDMTKEKEF YDEWPIKLGE
     VEPYKGPKTP DGREIIFYKI IDYILHGKEE INVIPSPPAD HWTLVSGLPT YVAENGFICN
     MLNAPADEYF TFQKGPVDET GWVIKNVLSL PIVNKKEDIV GVATFYNRKD GKPFDEHDEH
     ITETLTQFLG WSLLNTDTYE RVNKLESRKD IAQEMVMNLT KATPDEISSI LKFKEKLNVE
     VIEECEERQL LAILKEDLPD PRTADLYEFC FSDFPITEHE LVKCGLRLFL EINVVEKFKV
     PVEVLTRWMY TVRKGYRPVT YHNWRHGFNV GQTMFTLLMT GRLKKYYTDL EAFAMLAAAF
     CHDIDHRGTN NLYQMKSTSP LARLHGTSIL ERHHLEYSKT LLQDESLNIF QNLNKRQFET
     VIHLFEVAII ATDLALYFKK RTMFQKIVDT CEQMQSEEET IKYVTSDPTK KEVIMAMMMT
     ACDLSAITKP WEVQSQVALL VANEFWEQGD LERTVLQQQP IPMMDRSKKD ELPKLQVGFI
     DFVCTFVYKE FSRFHGEITP MLNGLQNNRV EWKSLAEEYE AKVKVTEEEA GKQEEEASDG
     KAATDLGGSA EDKKSKTCLM L
//